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| [[Image:1gru.gif|left|200px]] | | {{Seed}} |
| | [[Image:1gru.png|left|200px]] |
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| {{STRUCTURE_1gru| PDB=1gru | SCENE= }} | | {{STRUCTURE_1gru| PDB=1gru | SCENE= }} |
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| '''SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM'''
| | ===SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM=== |
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| ==Overview==
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| The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines. | | The line below this paragraph, {{ABSTRACT_PUBMED_11779463}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11779463 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11779463}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hsp60]] | | [[Category: Hsp60]] |
| [[Category: Molecular chaperone]] | | [[Category: Molecular chaperone]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:56:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:58:10 2008'' |